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http://purl.uniprot.org/citations/11387345http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11387345http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11387345http://www.w3.org/2000/01/rdf-schema#comment"We have reported previously the cloning and characterization of human and mouse protein kinase B gamma (PKB gamma), the third member of the PKB family of second messenger-regulated serine/threonine kinases (Brodbeck, D., Cron, P., and Hemmings, B. A. (1999) J. Biol. Chem. 274, 9133--9136). Here we report the isolation of human and mouse PKB gamma 1, a splice variant lacking the second regulatory phosphorylation site Ser-472 in the hydrophobic C-terminal domain. Expression of PKB gamma 1 is low compared with PKB gamma, and it is regulated in different human tissues. We show that PKB gamma and PKB gamma 1 differ in their response to stimulation by insulin, pervanadate, peroxide, or okadaic acid. Activation of PKB gamma 1 requires phosphorylation at a single regulatory site Thr-305. Interestingly, this site is phosphorylated to a higher extent in PKB gamma compared with PKB gamma 1 upon maximal stimulation by pervanadate, and this is reflected in the respective specific kinase activities. Furthermore, upon insulin stimulation of transfected cells, PKB gamma 1 translocates to the plasma membrane to a lesser extent than PKB gamma. Taken together, these results suggest that phosphorylation of the hydrophobic motif at the extreme C terminus of PKB gamma may facilitate translocation of the kinase to the membrane and/or its phosphorylation on the activation loop site by phosphoinositide-dependent protein kinase-1."xsd:string
http://purl.uniprot.org/citations/11387345http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m104633200"xsd:string
http://purl.uniprot.org/citations/11387345http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m104633200"xsd:string
http://purl.uniprot.org/citations/11387345http://purl.uniprot.org/core/author"Hemmings B.A."xsd:string
http://purl.uniprot.org/citations/11387345http://purl.uniprot.org/core/author"Hemmings B.A."xsd:string
http://purl.uniprot.org/citations/11387345http://purl.uniprot.org/core/author"Brodbeck D."xsd:string
http://purl.uniprot.org/citations/11387345http://purl.uniprot.org/core/author"Brodbeck D."xsd:string
http://purl.uniprot.org/citations/11387345http://purl.uniprot.org/core/author"Hill M.M."xsd:string
http://purl.uniprot.org/citations/11387345http://purl.uniprot.org/core/author"Hill M.M."xsd:string
http://purl.uniprot.org/citations/11387345http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11387345http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11387345http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/11387345http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/11387345http://purl.uniprot.org/core/pages"29550-29558"xsd:string
http://purl.uniprot.org/citations/11387345http://purl.uniprot.org/core/pages"29550-29558"xsd:string
http://purl.uniprot.org/citations/11387345http://purl.uniprot.org/core/title"Two splice variants of PKB gamma have different regulatory capacity depending on the presence or absence of the regulatory phosphorylation site Ser-472 in the C-terminal hydrophobic domain."xsd:string
http://purl.uniprot.org/citations/11387345http://purl.uniprot.org/core/title"Two splice variants of PKB gamma have different regulatory capacity depending on the presence or absence of the regulatory phosphorylation site Ser-472 in the C-terminal hydrophobic domain."xsd:string
http://purl.uniprot.org/citations/11387345http://purl.uniprot.org/core/volume"276"xsd:string
http://purl.uniprot.org/citations/11387345http://purl.uniprot.org/core/volume"276"xsd:string
http://purl.uniprot.org/citations/11387345http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11387345
http://purl.uniprot.org/citations/11387345http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11387345
http://purl.uniprot.org/citations/11387345http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/11387345
http://purl.uniprot.org/citations/11387345http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/11387345